Abstract:
:The membrane of mouse neuroblastoma N-18 cells degraded dynorphin-(1-13), dynorphin-(1-17), and Leu-enkephalin. The degradation of the former two peptides was inhibited strongly by N-ethylmaleimide, moderately by diisopropylphosphorofluoridate and phosphoramidon, and slightly by bestatin. When Leu-enkephalin was the substrate, however, the effects of phosphoramidon and bestatin were marked and those of N-ethylmaleimide and diisopropylphosphorofluoridate were negligibly small. Captopril did not affect the degradation of the two dynorphins and Leu-enkephalin, but inhibited the further cleavage of N-terminal fragments generated from dynorphin-(1-13) by the N-ethylmaleimide-sensitive protease. Thus, a cysteine protease and, probably, a serine protease are responsible to the initial fragmentation of the dynorphins.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Satoh M,Yokosawa H,Ishii Sdoi
10.1016/0006-291x(86)91095-8subject
Has Abstractpub_date
1986-10-15 00:00:00pages
335-41issue
1eissn
0006-291Xissn
1090-2104pii
0006-291X(86)91095-8journal_volume
140pub_type
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